Research workbench
Refined 1.8 ångströms resolution crystal structure of porcine epsilon-trypsin
Analyse Refined 1.8 ångströms resolution crystal structure of porcine epsilon-trypsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EPT
- Type
- protein
- Length
- 223 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Porcine E-trypsin
- EC
- 3.4.21.4
- UniProt
- P00761
- Ligands
- CA
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Porcine E-trypsin (EC 3.4.21.4) | protein | 43 | 7% helix, 49% strand | P00761 |
| B | Porcine E-trypsin (EC 3.4.21.4) | protein | 82 | 0% helix, 35% strand | P00761 |
| C | Porcine E-trypsin (EC 3.4.21.4) | protein | 98 | 20% helix, 33% strand | P00761 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–C · 2275 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 1910 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 1115 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00761
- Elsewhere: RCSB PDB 1EPT · PDBe 1EPT · UniProt P00761
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